Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q73CE0 (GLPK_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycerol kinase

EC=2.7.1.30
Alternative name(s):
ATP:glycerol 3-phosphotransferase
Glycerokinase
Short name=GK
Gene names
Name:glpK
Ordered Locus Names:BCE_1125
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Key enzyme in the regulation of glycerol uptake and metabolism. HAMAP MF_00186

Catalytic activity

ATP + glycerol = ADP + sn-glycerol 3-phosphate. HAMAP MF_00186

Pathway

Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. HAMAP MF_00186

Sequence similarities

Belongs to the FGGY kinase family.

Ontologies

Keywords
   Biological processGlycerol metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglycerol-3-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glycerol kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 510510Glycerol kinase HAMAP MF_00186
PRO_1000020699

Regions

Nucleotide binding410 – 4145ATP By similarity

Sites

Binding site121Substrate By similarity
Binding site161ATP By similarity
Binding site821Substrate By similarity
Binding site1341Substrate By similarity
Binding site2441Substrate By similarity
Binding site2661ATP By similarity
Binding site3091ATP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q73CE0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6ACBF18E0ABD8ACB

FASTA51056,912
        10         20         30         40         50         60 
MKKYILSLDQ GTTSSRAILX NKKGEIVHSA QKEFTQHFPK PGWVEHNAQE IWGSILAVIA 

        70         80         90        100        110        120 
TCLSEADVKP EQIAGIGITN QRETAVVWDK TTGKPIYNAI VWQSRQTAEI CDELKEKGYG 

       130        140        150        160        170        180 
EMVREKTGLL IDAYFSGTKV KWILDNVEGA REKAENGDLL FGTIDTWLVW KLSGGKAHVT 

       190        200        210        220        230        240 
DYSNASRTLM FNIHDLQWDD ELLDMLTVPK SMLPEVRPSS EVYGETIDYH FFGQNVPIAG 

       250        260        270        280        290        300 
VAGDQQAALF GQACFGEGMA KNTYGTGCFM LMNTGEKAVA SEHGLLTTIA WGIDGKVNYA 

       310        320        330        340        350        360 
LEGSIFVAGS AIQWLRDGMR MFKDASESEV YANRVESTDG VYVVPAFVGL GTPYWDSEVR 

       370        380        390        400        410        420 
GAMFGVTRGT TKEHFIRATL ESLAYQXKDV LCAMEADSGI ELKTLRVDGG AVKNNFLMKF 

       430        440        450        460        470        480 
QSDILDVPVE RPVINETTAL GAAYLAGLAV GYWKNQDEIK EQWHMDKRLN QQWKRKQAKS 

       490        500        510 
YMLDGKKQLK QQKLSNNHKQ CYNGDKLIIR 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS40056.1.
RefSeqNP_977448.1. NC_003909.8.

3D structure databases

HSSPHSSP built from PDB template 1XUP based on UniProtKB O34153.
ProteinModelPortalQ73CE0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ73CE0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000029401; EBBACP00000028751; EBBACG00000029392.
GeneID2750781.
GenomeReviewsGene locus BCE_1125 in contig AE017194_GR.
KEGGbca:BCE_1125.
NMPDRfig|222523.1.peg.1120.
PATRIC18851122. VBIBacCer118379_1066.
TIGRBCE_1125.

Phylogenomic databases

eggNOGCOG0554.
GeneTreeEBGT00050000001374.
HOGENOMHBG511469.
OMAALYGQLC.
ProtClustDBPRK00047.

Family and domain databases

HAMAPMF_00186. Glycerol_kin.
[Tree]
InterProIPR000577. Carb_kinase_FGGY.
IPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
KOK00864.
PANTHERPTHR10196. FGGY_kin. 1 hit.
PTHR10196:SF9. Glycerol_kin. 1 hit.
PfamPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01311. Glycerol_kin. 1 hit.
PROSITEPS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLPK_BACC1
AccessionPrimary (citable) accession number: Q73CE0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families